Cloning, Expression, and Characterization of a Glycoside Hydrolase Family 118 β-Agarase from Agarivorans sp. JA-1

Lee, Dong‐Geun; Jeon, Myong Je; Lee, Sang Hyeon

doi:10.4014/jmb.1209.09033

Cited by 22 publications

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“…Although several β-agarase genes that catalyze the hydrolysis of agar (reviewed in reference 3) have been identified in A. albus (4 –6) and Agarivorans sp. (6–11), there is no whole-genome sequence information available for the genus. We therefore undertook to characterize the genomic features of the genus Agarivorans , and we present here the draft genome sequence of A. albus strain MKT 106 T (1).…”

Section: Genome Announcementmentioning

confidence: 99%

Draft Genome Sequence of Agarivorans albus Strain MKT 106 ^T , an Agarolytic Marine Bacterium

et al. 2013

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Section: Genome Announcementmentioning

confidence: 99%

Draft Genome Sequence of Agarivorans albus Strain MKT 106 ^T , an Agarolytic Marine Bacterium

et al. 2013

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“…동일한 균주인 Agarivorans sp. JA-1에서 파 악한 다른 한천분해효소의 최적 pH는 GH-50 β-agarase 효소 가 pH 8.0이었고 [19], GH-118 β-agarase 효소는 pH 7.0이었 다 [14]. 그리고 β-agarase agaJA3와 아미노산 서열의 유사도가 높은 Vibrio sp.…”

Section: Catatggactgggataatatcccaattcc-3' (Inserted Aunclassified

Cloning, Expression, and Characterization of a Novel GH-16 β-Agarase from Agarivorans sp. JA-1

Jeon¹,

Kim²,

Lee³

et al. 2012

Journal of Life Science

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Authors report the glycoside hydrolase (GH) family 16 β-agarase from the strain of Agarivorans sp.JA-1, which authors previously stated as recombinant expression and characterization of GH-50 and GH-118 β-agarase. It comprised an open reading frame of 1,362 base pairs, which encodes a protein of 49,830 daltons consisting of 453 amino acid residues. Valuation of the total sequence showed that the enzyme has 98% nucleotide and 99% amino acid sequence similarities to those of GH-16 β-agarase from Pseudoalteromonas sp. CY24. The gene corresponding to a mature protein of 429 amino acids was recombinantly expressed in Escherichia coli, and the enzyme was purified to homogeneity by affinity chromatography. It showed maximal activity at 40°C and pH 5.0, representing 67.6 units/mg. Thin layer chromatography revealed that mainly neoagarohexaose and neoagarotetraose were produced from agarose. The enzyme would be valuable for the industrial production of functional neoagarooligosaccharides.

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“…β-agarases (EC 3.2.1.81) are the most common class of agarase and to date, more than 30 have been functionally verified and documented in the carbohydrate-active enzymes (CAZymes) database ( Chi et al, 2012 ). Based on amino acid sequence similarity, all β-agarases can be classified into the glycoside hydrolase (GH) subfamilies, including GH16, GH50, GH86, and GH118 ( Lee et al, 2012 ). The mechanism of these enzymes is well established ( Ekborg et al, 2006 ; Fu and Kim, 2010 ; Pluvinage et al, 2013 ; Yun et al, 2017 ).…”

Section: Introductionmentioning

confidence: 99%

Genome-Wide Identification and Functional Characterization of β-Agarases in Vibrio astriarenae Strain HN897

Liu

Jin

et al. 2020

Front. Microbiol.

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The genus Vibrio is a genetically and metabolically versatile group of heterotrophic bacteria that are important contributors to carbon cycling within marine and estuarine ecosystems. HN897, a Vibrio strain isolated from the coastal seawater of South China, was shown to be agarolytic and capable of catabolizing D -galactose. Herein, we used Illumina and PacBio sequencing to assemble the whole genome sequence for the strain HN897, which was comprised of two circular chromosomes (Vas1 and Vas2). Genome-wide phylogenetic analysis with 140 other Vibrio sequences firmly placed the strain HN897 into the Marisflavi clade, with Vibrio astriarenae strain C7 being the closest relative. Of all types of carbohydrate-active enzyme classes, glycoside hydrolases (GH) were the most common in the HN897 genome. These included eight GHs identified as putative β-agarases belonging to GH16 and GH50 families in equal proportions. Synteny analysis showed that GH16 and GH50 genes were tandemly arrayed on two different chromosomes consistent with gene duplication. Gene knockout and complementation studies and phenotypic assays confirmed that Vas1_1339 , a GH16_16 subfamily gene, exhibits an agarolytic phenotype of the strain. Collectively, these findings explained the agar-decomposing of strain HN897, but also provided valuable resources to gain more detailed insights into the evolution and physiological capability of the strain HN897, which was a presumptive member of the species V. astriarenae .

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Cloning, Expression, and Characterization of a Glycoside Hydrolase Family 118 β-Agarase from Agarivorans sp. JA-1

Cited by 22 publications

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Draft Genome Sequence of Agarivorans albus Strain MKT 106 ^T , an Agarolytic Marine Bacterium

Draft Genome Sequence of Agarivorans albus Strain MKT 106 ^T , an Agarolytic Marine Bacterium

Cloning, Expression, and Characterization of a Novel GH-16 β-Agarase from Agarivorans sp. JA-1

Genome-Wide Identification and Functional Characterization of β-Agarases in Vibrio astriarenae Strain HN897

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Cloning, Expression, and Characterization of a Glycoside Hydrolase Family 118 β-Agarase from Agarivorans sp. JA-1

Cited by 22 publications

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Draft Genome Sequence of Agarivorans albus Strain MKT 106 T , an Agarolytic Marine Bacterium

Draft Genome Sequence of Agarivorans albus Strain MKT 106 T , an Agarolytic Marine Bacterium

Cloning, Expression, and Characterization of a Novel GH-16 β-Agarase from Agarivorans sp. JA-1

Genome-Wide Identification and Functional Characterization of β-Agarases in Vibrio astriarenae Strain HN897

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Draft Genome Sequence of Agarivorans albus Strain MKT 106 ^T , an Agarolytic Marine Bacterium

Draft Genome Sequence of Agarivorans albus Strain MKT 106 ^T , an Agarolytic Marine Bacterium